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大肠杆菌50S核糖体上L7/L12的赖氨酸-51定位

Localization of Lys-51 of L7/L12 on 50S ribosomes from Escherichia coli.

作者信息

Maassen J A, Schop E N, Möller W

出版信息

Eur J Biochem. 1984 Jan 2;138(1):131-4. doi: 10.1111/j.1432-1033.1984.tb07891.x.

Abstract

Ribosomal protein L7/L12 from Escherichia coli was modified specifically at Lys-51 with 4-(6-formyl-3-azido-phenoxy)butyrimidate. Reconstitution of ribosomal cores, lacking L7/L12, with imidate-modified L7/L12 resulted in back formation of 50S particles which were fully active in elongation-factor-dependent processes. By use of the formylazidophenoxy moiety as hapten, the position of Lys-51 of L7/L12 on the 50S ribosome was determined by immune electron microscopy. The results show that an L7/L12 dimer is present in the L7/L12 stalk in such a way that Lys-51 is located at the far cytoplasmic end of the stalk. The experimental data are discussed in relation to a proposed model for the L7/L12 dimer.

摘要

来自大肠杆菌的核糖体蛋白L7/L12在赖氨酸-51处被4-(6-甲酰基-3-叠氮基苯氧基)丁酸亚胺酯特异性修饰。用亚胺酯修饰的L7/L12对缺乏L7/L12的核糖体核心进行重组,导致50S颗粒重新形成,这些颗粒在依赖延伸因子的过程中完全具有活性。通过使用甲酰叠氮基苯氧基部分作为半抗原,利用免疫电子显微镜确定了L7/L12的赖氨酸-51在50S核糖体上的位置。结果表明,L7/L12二聚体以赖氨酸-51位于柄的远细胞质端的方式存在于L7/L12柄中。结合提出的L7/L12二聚体模型对实验数据进行了讨论。

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